node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABQ93132.1 | ABQ93358.1 | PsycPRwf_0173 | PsycPRwf_0403 | PFAM: nitrogen regulatory protein P-II; Belongs to the P(II) protein family. | PFAM: glutamine amidotransferase, class-II; glutamate synthase, alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase. | 0.658 |
ABQ93132.1 | ABQ94585.1 | PsycPRwf_0173 | PsycPRwf_1645 | PFAM: nitrogen regulatory protein P-II; Belongs to the P(II) protein family. | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase, catalytic region; glutamine synthetase, beta-Grasp. | 0.545 |
ABQ93132.1 | ABQ94744.1 | PsycPRwf_0173 | PsycPRwf_1804 | PFAM: nitrogen regulatory protein P-II; Belongs to the P(II) protein family. | Signal transduction histidine kinase, nitrogen specific, NtrB; PFAM: ATP-binding region, ATPase domain protein domain protein; histidine kinase A domain protein domain protein. | 0.852 |
ABQ93132.1 | glnD | PsycPRwf_0173 | PsycPRwf_0556 | PFAM: nitrogen regulatory protein P-II; Belongs to the P(II) protein family. | Metal dependent phosphohydrolase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. | 0.814 |
ABQ93132.1 | glnE | PsycPRwf_0173 | PsycPRwf_0980 | PFAM: nitrogen regulatory protein P-II; Belongs to the P(II) protein family. | (Glutamate--ammonia-ligase) adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal tra [...] | 0.484 |
ABQ93358.1 | ABQ93132.1 | PsycPRwf_0403 | PsycPRwf_0173 | PFAM: glutamine amidotransferase, class-II; glutamate synthase, alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase. | PFAM: nitrogen regulatory protein P-II; Belongs to the P(II) protein family. | 0.658 |
ABQ93358.1 | ABQ93510.1 | PsycPRwf_0403 | PsycPRwf_0555 | PFAM: glutamine amidotransferase, class-II; glutamate synthase, alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase. | PFAM: aminotransferase, class I and II. | 0.569 |
ABQ93358.1 | ABQ94585.1 | PsycPRwf_0403 | PsycPRwf_1645 | PFAM: glutamine amidotransferase, class-II; glutamate synthase, alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase. | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase, catalytic region; glutamine synthetase, beta-Grasp. | 0.981 |
ABQ93358.1 | ABQ94744.1 | PsycPRwf_0403 | PsycPRwf_1804 | PFAM: glutamine amidotransferase, class-II; glutamate synthase, alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase. | Signal transduction histidine kinase, nitrogen specific, NtrB; PFAM: ATP-binding region, ATPase domain protein domain protein; histidine kinase A domain protein domain protein. | 0.479 |
ABQ93358.1 | glnD | PsycPRwf_0403 | PsycPRwf_0556 | PFAM: glutamine amidotransferase, class-II; glutamate synthase, alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase. | Metal dependent phosphohydrolase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. | 0.647 |
ABQ93358.1 | glnE | PsycPRwf_0403 | PsycPRwf_0980 | PFAM: glutamine amidotransferase, class-II; glutamate synthase, alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase. | (Glutamate--ammonia-ligase) adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal tra [...] | 0.571 |
ABQ93358.1 | guaB | PsycPRwf_0403 | PsycPRwf_1261 | PFAM: glutamine amidotransferase, class-II; glutamate synthase, alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase. | Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. | 0.602 |
ABQ93509.1 | ABQ93510.1 | PsycPRwf_0554 | PsycPRwf_0555 | PFAM: CBS domain containing protein; protein of unknown function DUF294, nucleotidyltransferase putative. | PFAM: aminotransferase, class I and II. | 0.485 |
ABQ93509.1 | glnD | PsycPRwf_0554 | PsycPRwf_0556 | PFAM: CBS domain containing protein; protein of unknown function DUF294, nucleotidyltransferase putative. | Metal dependent phosphohydrolase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. | 0.425 |
ABQ93510.1 | ABQ93358.1 | PsycPRwf_0555 | PsycPRwf_0403 | PFAM: aminotransferase, class I and II. | PFAM: glutamine amidotransferase, class-II; glutamate synthase, alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase. | 0.569 |
ABQ93510.1 | ABQ93509.1 | PsycPRwf_0555 | PsycPRwf_0554 | PFAM: aminotransferase, class I and II. | PFAM: CBS domain containing protein; protein of unknown function DUF294, nucleotidyltransferase putative. | 0.485 |
ABQ93510.1 | glnD | PsycPRwf_0555 | PsycPRwf_0556 | PFAM: aminotransferase, class I and II. | Metal dependent phosphohydrolase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. | 0.713 |
ABQ93510.1 | map | PsycPRwf_0555 | PsycPRwf_0557 | PFAM: aminotransferase, class I and II. | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.464 |
ABQ94585.1 | ABQ93132.1 | PsycPRwf_1645 | PsycPRwf_0173 | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase, catalytic region; glutamine synthetase, beta-Grasp. | PFAM: nitrogen regulatory protein P-II; Belongs to the P(II) protein family. | 0.545 |
ABQ94585.1 | ABQ93358.1 | PsycPRwf_1645 | PsycPRwf_0403 | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase, catalytic region; glutamine synthetase, beta-Grasp. | PFAM: glutamine amidotransferase, class-II; glutamate synthase, alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase. | 0.981 |